Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships.
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Confocal Spectroscopy to Study Dimerization, Oligomerization and Aggregation of Proteins: A Practical GuidePhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Dihydropyridine Derivatives Modulate Heat Shock Responses and have a Neuroprotective Effect in a Transgenic Mouse Model of Alzheimer's Disease.Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphataseEffects of Mutations on the Reconfiguration Rate of α-SynucleinTwo-Step Amyloid Aggregation: Sequential Lag Phase IntermediatesEarly amyloidogenic oligomerization studied through fluorescence lifetime correlation spectroscopy.Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.Supersaturation-limited amyloid fibrillation of insulin revealed by ultrasonication.Ultrafast propagation of β-amyloid fibrils in oligomeric cloud.Heat of supersaturation-limited amyloid burst directly monitored by isothermal titration calorimetry.Oxidative stress, mitochondrial damage and neurodegenerative diseasesThe structural basis for optimal performance of oligothiophene-based fluorescent amyloid ligands: conformational flexibility is essential for spectral assignment of a diversity of protein aggregates.Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.Water molecular system dynamics associated with amyloidogenic nucleation as revealed by real time near infrared spectroscopy and aquaphotomics.Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.A native interactor scaffolds and stabilizes toxic ATAXIN-1 oligomers in SCA1.Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid Fibrillation.Expanding rare disease drug trials based on shared molecular etiologyConserved features of intermediates in amyloid assembly determine their benign or toxic states.The keystone of Alzheimer pathogenesis might be sought in Aβ physiologyβ-Cell failure in type 2 diabetes: a case of asking too much of too few?Continuous and pulsed hydrogen-deuterium exchange and mass spectrometry characterize CsgE oligomerizationClusterin Binds to Aβ1-42 Oligomers with High Affinity and Interferes with Peptide Aggregation by Inhibiting Primary and Secondary Nucleation.Understanding protein aggregation from the view of monomer dynamicsStabilization, characterization, and selective removal of cystatin C amyloid oligomers.Structural insights into Aβ42 oligomers using site-directed spin labelingProbing amyloid protein aggregation with optical superresolution methods: from the test tube to models of disease.Divergent prion strain evolution driven by PrPC expression level in transgenic mice.Amyloid β-protein oligomers and Alzheimer's disease.α-Synuclein oligomers: an amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions.Information flow and protein dynamics: the interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations.Structural, morphological, and functional diversity of amyloid oligomers.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations.Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal InvasionBRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells.Polyanion binding accelerates the formation of stable and low-toxic aggregates of ALS-linked SOD1 mutant A4V.
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P2860
Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships.
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Protein misfolded oligomers: e ...... ucture-toxicity relationships.
@en
Protein misfolded oligomers: e ...... ucture-toxicity relationships.
@nl
type
label
Protein misfolded oligomers: e ...... ucture-toxicity relationships.
@en
Protein misfolded oligomers: e ...... ucture-toxicity relationships.
@nl
prefLabel
Protein misfolded oligomers: e ...... ucture-toxicity relationships.
@en
Protein misfolded oligomers: e ...... ucture-toxicity relationships.
@nl
P1476
Protein misfolded oligomers: e ...... ucture-toxicity relationships.
@en
P2093
Fabrizio Chiti
P304
P356
10.1016/J.CHEMBIOL.2012.02.003
P577
2012-03-01T00:00:00Z